Protein profile

KP13_04971

putative phenylacetic acid degradation NADH oxidoreductase paaE

Genome: KpKP13

Gene: AHE44856.1 paaE Structure source: AlphaFold + ColabFold UniProt A0A0H3GSN2
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Amino acids 356
Annotations 6
Features 43
PDB binders 1
Druggability 0.352

Overview

Basic information about this protein and its source genome.

Accession
KP13_04971
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
AHE44856.1 paaE
Status
annotated
Amino acids
356
Structure source
AlphaFold + ColabFold
GO
GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced. GO:0051537 Binding to a 2 iron, 2 sulfur (2Fe-2S) cluster; this cluster consists of two iron atoms, with two inorganic sulfur atoms found between the irons and acting as bridging ligands. GO:0010124 The chemical reactions and pathways resulting in the breakdown of phenylacetate. GO:0051536 Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms. GO:0050660 Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2. GO:0046872 Binding to a metal ion.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
26.708
Human E-value
1.63e-09
Gut microbiome off-target
hit
Essential (DEG)
N
DEG identity (%)
0.0
Localization
Cytoplasmic
ColabFold pLDDT
91.5

Selected Druggability evidence

AlphaFold / UniProt model

Selected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.

FPocket 0.352
Structure A0A0H3GSN2
Pocket Pocket 13
P2Rank 0.693
Structure A0A0H3GSN2
Pocket Pocket 1
ColabFold model
FPocket 0.414 · Pocket 2
P2Rank 0.668 · Pocket 1
Core conservation Accessory gene
Roary core
CoreCruncher accessory
Gut microbiome 47 / 4744 genomes with a hit
Normalized 0.01

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

6 GO

Gene Ontology (GO)

6
  • GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
  • GO:0051537 Binding to a 2 iron, 2 sulfur (2Fe-2S) cluster; this cluster consists of two iron atoms, with two inorganic sulfur atoms found between the irons and acting as bridging ligands.
  • GO:0010124 The chemical reactions and pathways resulting in the breakdown of phenylacetate.
  • GO:0051536 Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms.
  • GO:0050660 Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.
  • GO:0046872 Binding to a metal ion.

Sequence Features

Domain/signature hits from InterPro and related databases.

43 records
Show feature table
Start End DB Term Name
248 355 Gene3D G3DSA:3.10.20.30 -
248 355 InterPro IPR012675 Beta-grasp domain superfamily
94 242 SUPERFAMILY SSF52343 Ferredoxin reductase-like, C-terminal NADP-linked domain
94 242 InterPro IPR039261 Ferredoxin-NADP reductase (FNR), nucleotide-binding domain
101 242 Gene3D G3DSA:3.40.50.80 -
101 242 InterPro IPR039261 Ferredoxin-NADP reductase (FNR), nucleotide-binding domain
212 220 PRINTS PR00406 Cytochrome B5 reductase signature
91 105 PRINTS PR00406 Cytochrome B5 reductase signature
116 135 PRINTS PR00406 Cytochrome B5 reductase signature
262 354 ProSiteProfiles PS51085 2Fe-2S ferredoxin-type iron-sulfur binding domain profile.
262 354 InterPro IPR001041 2Fe-2S ferredoxin-type iron-sulfur binding domain
299 307 ProSitePatterns PS00197 2Fe-2S ferredoxin-type iron-sulfur binding region signature.
299 307 InterPro IPR006058 2Fe-2S ferredoxin, iron-sulphur binding site
270 342 Pfam PF00111 2Fe-2S iron-sulfur cluster binding domain
270 342 InterPro IPR001041 2Fe-2S ferredoxin-type iron-sulfur binding domain
245 352 FunFam G3DSA:3.10.20.30:FF:000023 3-ketosteroid-9-alpha-hydroxylase reductase subunit
4 351 NCBIfam TIGR02160 phenylacetate-CoA oxygenase/reductase subunit PaaK
4 351 InterPro IPR011884 Phenylacetate-CoA oxygenase/reductase, PaaK subunit
264 349 CDD cd00207 fer2
264 349 InterPro IPR001041 2Fe-2S ferredoxin-type iron-sulfur binding domain
2 100 Gene3D G3DSA:2.40.30.10 Translation factors
8 105 Pfam PF00970 Oxidoreductase FAD-binding domain
8 105 InterPro IPR008333 Flavoprotein pyridine nucleotide cytochrome reductase-like, FAD-binding domain
236 350 SUPERFAMILY SSF54292 2Fe-2S ferredoxin-like
236 350 InterPro IPR036010 2Fe-2S ferredoxin-like superfamily
2 106 ProSiteProfiles PS51384 Ferredoxin reductase-type FAD binding domain profile.
2 106 InterPro IPR017927 FAD-binding domain, ferredoxin reductase-type
212 220 PRINTS PR00371 Flavoprotein pyridine nucleotide cytochrome reductase signature
212 220 InterPro IPR001709 Flavoprotein pyridine nucleotide cytochrome reductase
36 46 PRINTS PR00371 Flavoprotein pyridine nucleotide cytochrome reductase signature
36 46 InterPro IPR001709 Flavoprotein pyridine nucleotide cytochrome reductase
116 135 PRINTS PR00371 Flavoprotein pyridine nucleotide cytochrome reductase signature
116 135 InterPro IPR001709 Flavoprotein pyridine nucleotide cytochrome reductase
55 62 PRINTS PR00371 Flavoprotein pyridine nucleotide cytochrome reductase signature
55 62 InterPro IPR001709 Flavoprotein pyridine nucleotide cytochrome reductase
141 150 PRINTS PR00371 Flavoprotein pyridine nucleotide cytochrome reductase signature
141 150 InterPro IPR001709 Flavoprotein pyridine nucleotide cytochrome reductase
4 244 CDD cd06214 PA_degradation_oxidoreductase_like
2 103 SUPERFAMILY SSF63380 Riboflavin synthase domain-like
2 103 InterPro IPR017938 Riboflavin synthase-like beta-barrel
4 349 PANTHER PTHR47354 NADH OXIDOREDUCTASE HCR
118 225 Pfam PF00175 Oxidoreductase NAD-binding domain
118 225 InterPro IPR001433 Oxidoreductase FAD/NAD(P)-binding

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

3D visualization script Full viewer

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Structural evidence

0 + 2

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry Method Resolution Chain Coverage Links Status
AlphaFold AF_A0A0H3GSN2
AlphaFold — — full sequence — Viewing
ColabFold KP13_04971
ColabFold — — full sequence — Loaded
Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET Sticks Spheres Surfaces Druggability Labels Zoom Positions
13 0.352

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK Sticks Spheres Surfaces Score Probability Labels Zoom Positions
1 8.13 0.433
2 2.73 0.082
3 2.2 0.053
4 2.05 0.045

Ligand evidence

Ligands grouped by evidence source. PDB ligands keep the source crystal visible, and loaded crystals can be opened directly in the structure viewer.

1 records

Structural evidence inferred from similar proteins. The source crystal indicates where the ligand was observed; the UniProt column identifies the homologous protein carrying that ligand.

Show only:
Ligand Source crystal UniProt (homolog) MW · LogP · TPSA Lipinski PAINS SMILES
FES
6LAA
A0A0K6ITW2 175.8 Da LogP 1.29 TPSA 0.0 ✓ Ro5 ✓ Clean S1[Fe]S[Fe]1

PDB and ChEMBL records on this protein are shown in full. ChEMBL records from similar proteins are capped at the top 100 per protein (by pchembl) and ZINC at the top 50 (Tanimoto ≥ 0.5). ADME columns are descriptor-based screening flags, not experimental toxicity results.